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D1ABJ5 (D1ABJ5_THECD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Tcur_1655
OrganismThermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081) [Complete proteome] [HAMAP] EMBL ACY97231.1
Taxonomic identifier471852 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Thermomonosporaceae › Thermomonospora ›

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1741Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2921Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2021Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium By similarity HAMAP-Rule MF_01338
Binding site1221Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1721Substrate By similarity HAMAP-Rule MF_01338
Binding site1761Substrate By similarity HAMAP-Rule MF_01338
Binding site2931Substrate By similarity HAMAP-Rule MF_01338
Binding site3251Substrate By similarity HAMAP-Rule MF_01338
Binding site3771Substrate By similarity HAMAP-Rule MF_01338
Site3321Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2001N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
D1ABJ5 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: 1CE218137AA205BA

FASTA48252,892
        10         20         30         40         50         60 
MSGNAGTGGR WSAGVIPYAE MGYWRPDYQP KDSDILAAFR ITPQPGVPPE EAGAAVAGES 

        70         80         90        100        110        120 
STATWTVVWT DRLTSYENYQ AKCYRVEPVP GQEGQFIAYI AYDLDLFEEG SIANLTSSII 

       130        140        150        160        170        180 
GNVFGFKALK ALRLEDMRIP PHYVKTFQGP PHGIVMEREY LGKYGRPLLG ATVKPKLGLS 

       190        200        210        220        230        240 
ARNYGRVVYE ALRGGLDFTK DDENINSQPF MRWRDRFLFC MEAVNKAQAA TGEIKGHYLN 

       250        260        270        280        290        300 
VTAATMEDMY ERAEFAKELG SVIVMIDLTI GYTAIQSMAK WARRNGVLLH LHRAGHSTYT 

       310        320        330        340        350        360 
RQKTHGVSFR VIAKWMRLAG VDHIHAGTVV GKLEGDPNSV AGYYDTLRLG KVPADPVKGL 

       370        380        390        400        410        420 
YFDQDWASLP GVMPVASGGI HAGQMHQLLH YLGEDVILQF GGGTIGHPMG IAAGATANRV 

       430        440        450        460        470        480 
ALEAMIKARN EGRDFLKEGP DILRAAAKHS RELDVALSTW GDVTFTYQST DTPDVVETPV 


SV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001738 Genomic DNA. Translation: ACY97231.1.
RefSeqYP_003299269.1. NC_013510.1.

3D structure databases

ProteinModelPortalD1ABJ5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACY97231; ACY97231; Tcur_1655.
GeneID8602976.
KEGGtcu:Tcur_1655.
PATRIC32512914. VBITheCur33965_1691.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD1ABJ5_THECD
AccessionPrimary (citable) accession number: D1ABJ5
Entry history
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: May 1, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info